Reviewed,
UniProtKB/Swiss-Prot O49886 (CYPH_LUPLU)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Peptidyl-prolyl cis-trans isomerase Short name=PPIase Short name=Rotamase EC=5.2.1.8 Alternative name(s): Cyclophilin Cyclosporin A-binding protein |
| Organism | Lupinus luteus (European yellow lupin) |
| Taxonomic identifier | 3873 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Genisteae › Lupinus |
Protein attributes
| Sequence length | 172 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
| Catalytic activity | Peptidylproline (omega=180) = peptidylproline (omega=0). |
| Enzyme regulation | Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase. |
| Subcellular location | |
| Tissue specificity | Expressed in meristematic tissues, with higher levels in nodules. Ref.1 |
| Sequence similarities | Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Cyclosporin |
| Molecular function | Isomerase Rotamase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | protein folding Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 172 | 172 | Peptidyl-prolyl cis-trans isomerase | PRO_0000064144 | ||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||
| Domain | 7 – 170 | 164 | PPIase cyclophilin-type | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 5 – 12 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 15 – 24 | 10 | ||||||||||||||||||||||||||||||||||||||
| Turn | 26 – 28 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 30 – 41 | 12 | ||||||||||||||||||||||||||||||||||||||
| Turn | 42 – 44 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 50 – 53 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 62 – 64 | 3 | ||||||||||||||||||||||||||||||||||||||
| Turn | 65 – 67 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 68 – 71 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 74 – 80 | 7 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 104 – 107 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 124 | 6 | ||||||||||||||||||||||||||||||||||||||
| Helix | 127 – 129 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 135 – 141 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 143 – 151 | 9 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 155 – 157 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 163 – 170 | 8 | ||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Yellow lupine cyclophilin transcripts are highly accumulated in the nodule meristem zone." Nuc K., Nuc P., Slomski R. Mol. Plant Microbe Interact. 14:1384-1394(2001) [PubMed: 11768533] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY. Strain: cv. Ventus. Tissue: Seedling. |
| [2] | "Theoretical model of CYPH_LUPLU." Siddharhta K. Submitted (AUG-2002) to the PDB data bank Cited for: 3D-STRUCTURE MODELING. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Y16088 mRNA. Translation: CAA76054.1. AF178458 Genomic DNA. Translation: AAF00471.1. | |||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| SMR | O49886. Positions 1-171. | ||||||||||||
| ModBase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 5.2.1.8. 261. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR002130. PPIase_cyclophilin. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit. | ||||||||||||
| Pfam | PF00160. Pro_isomerase. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00153. CSAPPISMRASE. | ||||||||||||
| PROSITE | PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | CYPH_LUPLU | ||||||||
| Accession | Primary (citable) accession number: O49886 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


